Phosphorylation of an N-terminal regulatory domain activates the CheB methylesterase in bacterial chemotaxis

A. Lupas, J. Stock

Research output: Contribution to journalArticle

133 Scopus citations

Abstract

Two types of reversible protein modification reactions have been identified in bacterial chemotaxis, methylation of membrane receptor-transducer proteins at glutamate side chains and phosphorylation of cytoplasmic signal transduction proteins at histidine and aspartate side chains. CheB is a bifunctional enzyme that is involved in both these modification processes. Its C-terminal domain is a methylesterase that catalyzes the hydrolysis of γ-carboxyl glutamyl methyl esters in the cytoplasmic domain of chemoreceptor proteins. Its N-terminal domain is a phosphatase that catalyzes the hydrolysis of phospho-CheA, the central response regulator of bacterial chemotaxis. Phospho-CheB, produced as an intermediate in the phosphatase reaction, has dramatically increased methylesterase activity. The interplay between the methylesterase and phosphatase activities of CheB may provide a crucial link between adaptation and excitation in stimulus-response coupling.

Original languageEnglish (US)
Pages (from-to)17337-17342
Number of pages6
JournalJournal of Biological Chemistry
Volume264
Issue number29
StatePublished - Jan 1 1989

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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